title: Isolation and characterization of recombinant eel growth hormone expressed in Escherichia coli.
abstract: To obtain information about the microheterogeneity of recombinant protein, recombinant eel growth hormone II (EGH) analogues expressed in Escherichia coli were isolated and characterized. The modification was classified into three types: monodeamidation of Asn, oxidation of Met and N-terminal formylation. Monodeamidated EGH was isolated by ion-exchange chromatography. The major deamidation site (Asn 147) was determined by peptide mapping using the substrate specificity of trypsin. Oxidized EGH and N-terminal-formylated EGH were isolated by reversed-phase high-performance liquid chromatography. Oxidized EGH was identified by amino acid composition analysis and N-terminal-formylated peptide by mass spectrometry.
authors.affiliation: Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Japan.
authors.forename: S
authors.initials: S
authors.lastname: Sugimoto
authors.forename: K
authors.initials: K
authors.lastname: Yamaguchi
authors.forename: Y
authors.initials: Y
authors.lastname: Yokoo
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004524:Eels / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D013006:Growth Hormone / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D011995:Recombination, Genetic
chemical_list: D013006:Growth Hormone